Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
JR Lepock, KP Ritchie, MC Kolios, AM Rodahl… - Biochemistry, 1992 - ACS Publications
JR Lepock, KP Ritchie, MC Kolios, AM Rodahl, KA Heinz, J Kruuv
Biochemistry, 1992•ACS PublicationsRevised Manuscript Received October 2, 1992 abstract: The thermodynamic parameters
characterizing protein folding can be obtained directly using differential scanning calorimetry
(DSC). They are meaningful only for reversible unfolding at equilibrium, which holds for
small globular proteins; however, the unfolding or denaturation of most large, multidomain or
multisubunit proteins is either partially or totally irreversible. The simplest kinetic model
describing partially irreversible denaturation requires three states:
characterizing protein folding can be obtained directly using differential scanning calorimetry
(DSC). They are meaningful only for reversible unfolding at equilibrium, which holds for
small globular proteins; however, the unfolding or denaturation of most large, multidomain or
multisubunit proteins is either partially or totally irreversible. The simplest kinetic model
describing partially irreversible denaturation requires three states:
Revised Manuscript Received October 2, 1992 abstract: The thermodynamic parameters characterizing protein folding can be obtained directly using differential scanning calorimetry (DSC). They are meaningful only for reversible unfolding at equilibrium, which holds for small globular proteins; however, the unfolding or denaturation of most large, multidomain or multisubunit proteins is either partially or totally irreversible. The simplest kinetic model describing partially irreversible denaturation requires three states:
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